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Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone

Hsp90 is a ubiquitous molecular chaperone. Previous structural analysis demonstrated that Hsp90 can adopt a large number of structurally distinct conformations, however the functional role of this flexibility is not understood. Here we investigate the structural consequences of substrate binding wit...

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Autori principali: Street, Timothy O., Lavery, Laura A., Agard, David A.
Natura: Artigo
Lingua:Inglês
Pubblicazione: 2011
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Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC3105473/
https://ncbi.nlm.nih.gov/pubmed/21474071
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.molcel.2011.01.029
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